3.1.31.1: micrococcal nuclease
This is an abbreviated version!
For detailed information about micrococcal nuclease, go to the full flat file.
Word Map on EC 3.1.31.1
-
3.1.31.1
-
chromatin
-
nucleosomes
-
histone
-
nuclei
-
strand
-
nucleases
-
mononucleosomes
-
dnaase
-
deoxyribonuclease
-
footprint
-
coagulase
-
nucleoprotein
-
enterotoxin
-
nonhistone
-
oligonucleosomes
-
octamer
-
ribonucleoprotein
-
polycephalum
-
chromatin-associated
-
non-transcribed
-
medicine
-
protein-dna
-
globin
-
staphylococci
-
native-like
-
internucleosomal
-
hyperacetylated
-
snrnp
-
telomeres
-
nuclease-resistant
-
32p-postlabeling
-
decondensation
-
physarum
-
minichromosome
-
chromatin-bound
-
endonucleolytic
-
coagulase-positive
-
coagulase-negative
-
end-labeling
-
histone-dna
-
beta-globin
-
drug development
-
molecular biology
-
superhelical
-
supercoiled
-
exonuclease
-
dielectric
-
analysis
-
i-hypersensitive
-
ladder
-
base-pairs
-
biotechnology
-
cscl
-
heterochromatic
-
nucleolytic
- 3.1.31.1
- chromatin
- nucleosomes
- histone
- nuclei
- strand
- nucleases
-
mononucleosomes
- dnaase
- deoxyribonuclease
-
footprint
- coagulase
- nucleoprotein
- enterotoxin
-
nonhistone
-
oligonucleosomes
-
octamer
- ribonucleoprotein
- polycephalum
-
chromatin-associated
-
non-transcribed
- medicine
-
protein-dna
- globin
-
staphylococci
-
native-like
-
internucleosomal
-
hyperacetylated
-
snrnp
-
telomeres
-
nuclease-resistant
-
32p-postlabeling
-
decondensation
- physarum
-
minichromosome
-
chromatin-bound
-
endonucleolytic
-
coagulase-positive
-
coagulase-negative
-
end-labeling
-
histone-dna
- beta-globin
- drug development
- molecular biology
-
superhelical
-
supercoiled
-
exonuclease
-
dielectric
- analysis
-
i-hypersensitive
-
ladder
-
base-pairs
- biotechnology
- cscl
-
heterochromatic
-
nucleolytic
Reaction
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products =
Synonyms
AtTSN1, AtTSN2, cTSN, EC 3.1.4.7, Epstein-Barr virusencoded transcription factor 2 co-activator p100, HsTSN, micrococcal DNase, micrococcal endonuclease, Micrococcal nuclease, MN, MN ase, MNase, Nuc, NUC1, Nuc2, nucB, nuclease 8V, nuclease T, nuclease T', nuclease, micrococcal, nuclease, staphylococcal, NucM, P100, PaTSN, PfTSN, ribonucleate (deoxyribo-nucleate) 3'-nucleotidohydrolase, ribonucleate (deoxyribonucleate) 3'-nucleotidohydrolase, S. aureus nuclease, SNA, snake venom phosphodiesterase, SNase, SNAseR, SND1, spleen endonuclease, spleen phosphodiesterase, staph nuclease, staphylococcal nuclease, Staphylococcal nuclease A, Staphylococcal nuclease domain containing-1, staphylococcal nuclease domain-containing 1, staphylococcal nuclease domain-containing protein 1, staphylococcus aureus nuclease, staphylococcus aureus nuclease B, Staphylococcus aureus nuclease homologue, thermonuclease, TNase, TSN, tudor staphylococcal nuclease, Tudor-SN, Tudor-staphylococcal nuclease
ECTree
3.1.31.1 micrococcal nucleaseAdvanced search results
results (
results (Temperature Stability
Temperature Stability on EC 3.1.31.1 - micrococcal nuclease
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
TEMPERATURE STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
15 - 80
-
temperature range for studying the thermal unfolding transitions
39
-
Tm-value of mutant enzyme W140F is 39.1°C, Tm-value of mutant enzyme W140Y is 38.6°C
48
51
51.7
-
melting point of K45C mutant with bound 5,5'-dithiobis-2-nitrobenzoic acid label
53
75
90
-
pH 7.9-8.8, 15 min, 20% loss of activity, pH 3.5 and 9.6, 15 min, 50% loss of activity
additional information
75
1 h, heat-treated isozyme Nuc1 is still able to degrade the DNA substrate
75
1 h, heat-treated isozyme Nuc2 is still able to degrade the DNA substrate
additional information
-
heat-stable extracellular enzyme related structurally to a heat-labile cellular nuclease
additional information
-
2-O-alpha-mannosylglycerate protects against thermal denaturation. 0.5 M 2-O-alpha-mannosylglycerate increases Tm-value by 7.1°C. 0.5 M glycerol or trehalose increase the Tm-value by 0.8°C and 4.2°C, respectively
additional information
-
different concentrations of mannosylglycerate or presence of urea at 0.25M show no correlation with changes in the thermodynamic stability of the P117G/H124L/S128A mutant enzyme
additional information
temperature- and pressure-dependent stability diagram, thermodynamic properties, and folding reaction kinetics of the small, single-domain monomeric staphylococcal nuclease in presence or absence of macromolecular crowder agent Ficoll PM 70, which behaves as a semi-rigid spheroid with a hydrodynamic radius of about 5 nm, detailed overview. Increasing the temperature from 25°C to 57°C exhibits no change of the size of the crowder particles within the experimentalerror. No significant changes in particle size are detected by raising the pressure up to 2.5 kbar. The measured translational diffusion times indicate that, depending on the size of the protein, themicroviscosity of Ficoll PM70 is only about 4-6 times larger than the microviscosity of pure water
additional information
-
examination of denaturation (monitored by intrinsic fluorescence of Trp140) due to heat (pH 7): D21N/T33V/T41I/S59A/P117G/A128A mutant(Tm = 72°C), K9A mutant (Tm = 71°C), E73A mutant (Tm = 67°C), E75A mutant (Tm = 70°C), E75Q mutant (Tm = 70°C), D77A mutant (Tm = 67°C), Y91A mutant (Tm = 58°C), Y93A mutant (Tm = 52°C), E101A mutant (Tm = 71°C), K127A mutant (Tm = 75°C), A128S mutant (Tm = 71°C)
